Evidence for Distinct Roles in Catalysis for Residues of the Serine-Serine-Lysine Catalytic Triad of Fatty Acid Amide Hydrolase
Open Access
- 1 September 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (39) , 37393-37399
- https://doi.org/10.1074/jbc.m303922200
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Structural Adaptations in a Membrane Enzyme That Terminates Endocannabinoid SignalingScience, 2002
- Comparative Characterization of a Wild Type and Transmembrane Domain-Deleted Fatty Acid Amide Hydrolase: Identification of the Transmembrane Domain as a Site for OligomerizationBiochemistry, 1998
- Study of the amidase signature groupBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1996
- Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amidesNature, 1996
- Aeropyrum pernix gen. nov., sp. nov., a Novel Aerobic Hyperthermophilic Archaeon Growing at Temperatures up to 100 CInternational Journal of Systematic and Evolutionary Microbiology, 1996
- Isolation and Structure of a Brain Constituent That Binds to the Cannabinoid ReceptorScience, 1992
- An investigation into the minimum requirements for peptide hydrolysis by mutation of the catalytic triad of trypsinJournal of the American Chemical Society, 1992
- Probing the mechanism and improving the rate of substrate-assisted catalysis in subtilisin BPN'Biochemistry, 1991
- The Catalytic Role of the Active Site Aspartic Acid in Serine ProteasesScience, 1987
- Spectrophotometric Investigations of the Mechanism of α-Chymotrypsin-catalyzed Hydrolyses. Detection of the Acyl-enzyme Intermediate1-3Journal of the American Chemical Society, 1962